ID A0A0F0IJS0_ASPPU Unreviewed; 573 AA.
AC A0A0F0IJS0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03106};
DE EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_03106};
DE AltName: Full=ATP-sulfurylase {ECO:0000256|HAMAP-Rule:MF_03106};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_03106};
DE Short=SAT {ECO:0000256|HAMAP-Rule:MF_03106};
GN Name=MET3 {ECO:0000256|HAMAP-Rule:MF_03106};
GN ORFNames=P875_00108859 {ECO:0000313|EMBL:KJK67935.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK67935.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK67935.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first intracellular reaction of sulfate
CC assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic
CC sulfate and ATP. Plays an important role in sulfate activation as a
CC component of the biosynthesis pathway of sulfur-containing amino acids.
CC {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03106};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by 3'-phosphoadenosine
CC 5'-phosphosulfate (PAPS). {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000256|HAMAP-
CC Rule:MF_03106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- DOMAIN: The adenylyl-sulfate kinase (APS kinase) is non-functional. It
CC is involved in allosteric regulation by PAPS. PAPS binding induces a
CC large rotational rearrangement of domains lowering the substrate
CC affinity of the enzyme. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC family. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJK67935.1}.
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DR EMBL; JZEE01000155; KJK67935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0IJS0; -.
DR STRING; 1403190.A0A0F0IJS0; -.
DR UniPathway; UPA00097; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1.
DR HAMAP; MF_03106; Sulf_adenylyltr_euk; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR027535; Sulf_adenylyltr_euk.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR NCBIfam; TIGR00455; apsK; 1.
DR NCBIfam; TIGR00339; sopT; 1.
DR PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW Rule:MF_03106}; Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03106};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192, ECO:0000256|HAMAP-
KW Rule:MF_03106}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_03106};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03106};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_03106}; Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03106}.
FT DOMAIN 4..164
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 174..387
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT REGION 1..169
FT /note="N-terminal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT REGION 395..573
FT /note="Allosteric regulation domain; adenylyl-sulfate
FT kinase-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT ACT_SITE 198
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT ACT_SITE 199
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT ACT_SITE 200
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 197..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 197
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 199
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 291..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 295
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 434..437
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 515
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT SITE 203
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT SITE 206
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT SITE 330
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
SQ SEQUENCE 573 AA; 63872 MW; E10CE8A1FAF9A60C CRC64;
MANTPHGGVL KDLLARDAPR HDQLAAEAES LPAIVLSERQ LCDLELIMNG GFSPLEGFMN
QKDFDGVCEN CRLADGNLFS MPITLDASQQ LISELKLQAG SRVTLRDFRD DRNLAILTID
DIYRADKEKE AKLVFGGDPE HPAIKYLNTK VEEFYIGGKI EAVNKLNHYD YVALRYTPAE
LRIHFDKLGW SRVVAFQTRN PMHRAHRELT VRAARARAAN VLIHPVVGLT KPGDIDHFTR
VRAYQALLPR YPNGMAVLGL LGLAMRMGGP REAIWHAIIR KNHGATHFIV GRDHAGPGKN
SKGEEFYGPY DAQHAVEKYK DELGIEVVEF QQVTYLPDTD EYKPKDEVPA GVKTLDISGT
ELRNRLRTGA HIPEWFSYPE VVKILRESSP PRNTQGFTVF LTGYQNSGKD AIARALQVTL
NQQGGRAVSL LLGDTVRHEL SSELGFSRED RHTNIQRIAF VASELTKAGA AVIAAPIAPY
EHSRKAAREA VSQHGSFFLV HVNTPLEYCE KTDKRGIYAK ARAGEIKGFT GVDDPYEAPE
NAHLTVDVSK QSVRSIVHEI ILLLETEGFF DRA
//
